New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0).
Adenosine triphosphate, ATP, is the energy currency of living cells. While ATP synthases of archae and ATP synthases of pro- and eukaryotic organisms operate as energy producers by synthesizing ATP, the eukaryotic V-ATPase hydrolyzes ATP and thus functions as energy transducer. These enzymes share features like the hydrophilic catalytic- and the membrane-embedded ion-translocating sector, allowing them to operate as nano-motors and to transform the transmembrane electrochemical ion gradient into ATP or vice versa. Since archaea are rooted close to the origin of life, the A-ATP synthase is probably more similar in its composition and function to the "original" enzyme, invented by Nature billion years ago. On the contrary, the V-ATPases have acquired specific structural, functional and regulatory features during evolution. This review will summarize the current knowledge on the structure, mechanism and regulation of A-ATP synthases and V-ATPases. The importance of V-ATPase in pathophysiology of diseases will be discussed.
Grüber
Gerhard
G
School of Biological Sciences, Nanyang Technological University, Singapore, Republic of Singapore. ggrueber@ntu.edu.sg
Marshansky
Vladimir
V
D000255:Adenosine Triphosphate / Q000737:chemistry; D001105:Archaea / Q000378:metabolism*; D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods; D004563:Electrochemistry / Q000379:methods; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008968:Molecular Conformation; D036103:Nanotechnology / Q000379:methods; D009711:Nucleotides / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000502:physiology*
D009711:Nucleotides; D000255:Adenosine Triphosphate; D025262:Vacuolar Proton-Translocating ATPases